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9.B.119.1.1
β-glucan synthase component, Fks1

Accession Number:P38631
Protein Name:1,3-beta-glucan synthase component FKS1
Length:1876
Molecular Weight:214851.00
Species:Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [559292]
Number of TMSs:16
Location1 / Topology2 / Orientation3: Mitochondrion1
Substrate Unknown

Cross database links:

Genevestigator: P38631
eggNOG: NOG307043
HEGENOM: HOG000216604
DIP: DIP-5749N
Entrez Gene ID: 851055   
Pfam: PF02364   
KEGG: sce:YLR342W   

Gene Ontology

GO:0000148 C:1,3-beta-D-glucan synthase complex
GO:0030478 C:actin cap
GO:0030479 C:actin cortical patch
GO:0016021 C:integral to membrane
GO:0005624 C:membrane fraction
GO:0005739 C:mitochondrion
GO:0003843 F:1,3-beta-D-glucan synthase activity
GO:0005515 F:protein binding
GO:0006075 P:(1->3)-beta-D-glucan biosynthetic process
GO:0007047 P:cellular cell wall organization
GO:0045807 P:positive regulation of endocytosis
GO:0008360 P:regulation of cell shape
GO:0008361 P:regulation of cell size

References (20)

[1] “The yeast FKS1 gene encodes a novel membrane protein, mutations in which confer FK506 and cyclosporin A hypersensitivity and calcineurin-dependent growth.”  Eng W.-K.et.al.   7530227
[2] “The Saccharomyces cerevisiae FKS1 (ETG1) gene encodes an integral membrane protein which is a subunit of 1,3-beta-D-glucan synthase.”  Douglas C.M.et.al.   7528927
[3] “Characterization and gene cloning of 1,3-beta-D-glucan synthase from Saccharomyces cerevisiae.”  Inoue S.B.et.al.   7649185
[4] “Identification of two cell cycle regulated genes affecting the beta 1,3-glucan content of cell walls in Saccharomyces cerevisiae.”  Ram A.F.J.et.al.   7828729
[5] “Papulacandin B resistance in budding and fission yeasts: isolation and characterization of a gene involved in (1,3)beta-D-glucan synthesis in Saccharomyces cerevisiae.”  Castro C.et.al.   7592316
[6] “Calcineurin, the Ca2+/calmodulin-dependent protein phosphatase, is essential in yeast mutants with cell integrity defects and in mutants that lack a functional vacuolar H(+)-ATPase.”  Garrett-Engele P.et.al.   7542741
[7] “FKS1 mutations responsible for selective resistance of Saccharomyces cerevisiae to the novel 1,3-beta-glucan synthase inhibitor arborcandin C.”  Ohyama T.et.al.   14693557
[8] “The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.”  Johnston M.et.al.   9169871
[9] “Calcineurin-dependent growth of an FK506- and CsA-hypersensitive mutant of Saccharomyces cerevisiae.”  Parent S.A.et.al.   7510323
[10] “Differential expression and function of two homologous subunits of yeast 1,3-beta-D-glucan synthase.”  Mazur P.et.al.   7565718
[11] “In vitro activity of 1,3-beta-D-glucan synthase requires the GTP-binding protein Rho1.”  Mazur P.et.al.   8662910
[12] “Identification of yeast Rho1p GTPase as a regulatory subunit of 1,3-beta-glucan synthase.”  Qadota H.et.al.   8602515
[13] “Movement of yeast 1,3-beta-glucan synthase is essential for uniform cell wall synthesis.”  Utsugi T.et.al.   11856368
[14] “Dissection of upstream regulatory components of the Rho1p effector, 1,3-beta-glucan synthase, in Saccharomyces cerevisiae.”  Sekiya-Kawasaki M.et.al.   12399379
[15] “Mutations in Fks1p affect the cell wall content of beta-1,3- and beta-1,6-glucan in Saccharomyces cerevisiae.”  Dijkgraaf G.J.P.et.al.   12185837
[16] “A subset of membrane-associated proteins is ubiquitinated in response to mutations in the endoplasmic reticulum degradation machinery.”  Hitchcock A.L.et.al.   14557538
[17] “The proteome of Saccharomyces cerevisiae mitochondria.”  Sickmann A.et.al.   14576278
[18] “Analysis of beta-1,3-glucan assembly in Saccharomyces cerevisiae using a synthetic interaction network and altered sensitivity to caspofungin.”  Lesage G.et.al.   15166135
[19] “Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.”  Reinders J.et.al.   16823961
[20] “A multidimensional chromatography technology for in-depth phosphoproteome analysis.”  Albuquerque C.P.et.al.   18407956

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MNTDQQPYQG QTDYTQGPGN GQSQEQDYDQ YGQPLYPSQA DGYYDPNVAA GTEADMYGQQ 
61:	PPNESYDQDY TNGEYYGQPP NMAAQDGENF SDFSSYGPPG TPGYDSYGGQ YTASQMSYGE 
121:	PNSSGTSTPI YGNYDPNAIA MALPNEPYPA WTADSQSPVS IEQIEDIFID LTNRLGFQRD 
181:	SMRNMFDHFM VLLDSRSSRM SPDQALLSLH ADYIGGDTAN YKKWYFAAQL DMDDEIGFRN 
241:	MSLGKLSRKA RKAKKKNKKA MEEANPEDTE ETLNKIEGDN SLEAADFRWK AKMNQLSPLE 
301:	RVRHIALYLL CWGEANQVRF TAECLCFIYK CALDYLDSPL CQQRQEPMPE GDFLNRVITP 
361:	IYHFIRNQVY EIVDGRFVKR ERDHNKIVGY DDLNQLFWYP EGIAKIVLED GTKLIELPLE 
421:	ERYLRLGDVV WDDVFFKTYK ETRTWLHLVT NFNRIWVMHI SIFWMYFAYN SPTFYTHNYQ 
481:	QLVDNQPLAA YKWASCALGG TVASLIQIVA TLCEWSFVPR KWAGAQHLSR RFWFLCIIFG 
541:	INLGPIIFVF AYDKDTVYST AAHVVAAVMF FVAVATIIFF SIMPLGGLFT SYMKKSTRRY 
601:	VASQTFTAAF APLHGLDRWM SYLVWVTVFA AKYSESYYFL VLSLRDPIRI LSTTAMRCTG 
661:	EYWWGAVLCK VQPKIVLGLV IATDFILFFL DTYLWYIIVN TIFSVGKSFY LGISILTPWR 
721:	NIFTRLPKRI YSKILATTDM EIKYKPKVLI SQVWNAIIIS MYREHLLAID HVQKLLYHQV 
781:	PSEIEGKRTL RAPTFFVSQD DNNFETEFFP RDSEAERRIS FFAQSLSTPI PEPLPVDNMP 
841:	TFTVLTPHYA ERILLSLREI IREDDQFSRV TLLEYLKQLH PVEWECFVKD TKILAEETAA 
901:	YEGNENEAEK EDALKSQIDD LPFYCIGFKS AAPEYTLRTR IWASLRSQTL YRTISGFMNY 
961:	SRAIKLLYRV ENPEIVQMFG GNAEGLEREL EKMARRKFKF LVSMQRLAKF KPHELENAEF 
1021:	LLRAYPDLQI AYLDEEPPLT EGEEPRIYSA LIDGHCEILD NGRRRPKFRV QLSGNPILGD 
1081:	GKSDNQNHAL IFYRGEYIQL IDANQDNYLE ECLKIRSVLA EFEELNVEQV NPYAPGLRYE 
1141:	EQTTNHPVAI VGAREYIFSE NSGVLGDVAA GKEQTFGTLF ARTLSQIGGK LHYGHPDFIN 
1201:	ATFMTTRGGV SKAQKGLHLN EDIYAGMNAM LRGGRIKHCE YYQCGKGRDL GFGTILNFTT 
1261:	KIGAGMGEQM LSREYYYLGT QLPVDRFLTF YYAHPGFHLN NLFIQLSLQM FMLTLVNLSS 
1321:	LAHESIMCIY DRNKPKTDVL VPIGCYNFQP AVDWVRRYTL SIFIVFWIAF VPIVVQELIE 
1381:	RGLWKATQRF FCHLLSLSPM FEVFAGQIYS SALLSDLAIG GARYISTGRG FATSRIPFSI 
1441:	LYSRFAGSAI YMGARSMLML LFGTVAHWQA PLLWFWASLS SLIFAPFVFN PHQFAWEDFF 
1501:	LDYRDYIRWL SRGNNQYHRN SWIGYVRMSR ARITGFKRKL VGDESEKAAG DASRAHRTNL 
1561:	IMAEIIPCAI YAAGCFIAFT FINAQTGVKT TDDDRVNSVL RIIICTLAPI AVNLGVLFFC 
1621:	MGMSCCSGPL FGMCCKKTGS VMAGIAHGVA VIVHIAFFIV MWVLESFNFV RMLIGVVTCI 
1681:	QCQRLIFHCM TALMLTREFK NDHANTAFWT GKWYGKGMGY MAWTQPSREL TAKVIELSEF 
1741:	AADFVLGHVI LICQLPLIII PKIDKFHSIM LFWLKPSRQI RPPIYSLKQT RLRKRMVKKY 
1801:	CSLYFLVLAI FAGCIIGPAV ASAKIHKHIG DSLDGVVHNL FQPINTTNND TGSQMSTYQS 
1861:	HYYTHTPSLK TWSTIK